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Literature summary for 3.2.2.9 extracted from

  • Harijan, R.K.; Hoff, O.; Ducati, R.G.; Firestone, R.S.; Hirsch, B.M.; Evans, G.B.; Schramm, V.L.; Tyler, P.C.
    Selective inhibitors of Helicobacter pylori methylthioadenosine nucleosidase and human methylthioadenosine phosphorylase (2019), J. Med. Chem., 62, 3286-3296 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
structure in complex with transition state analogue inhibitors Helicobacter pylori

Inhibitors

Inhibitors Comment Organism Structure
(4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(ethynylsulfanyl)methyl]pyrrolidin-3-ol transition-state analogue, shows significant overlap in specificity with human 5'-methylthioadenosine phosphorylase MTAP Helicobacter pylori
(4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[[(pent-4-yn-1-yl)sulfanyl]methyl]pyrrolidin-3-ol transition-state analogue, best binding inhibitor tested, shows significant overlap in specificity with human 5'-methylthioadenosine phosphorylase MTAP Helicobacter pylori

Organism

Organism UniProt Comment Textmining
Helicobacter pylori A0A1W0VQJ9
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Synonyms

Synonyms Comment Organism
BW246_00770
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Helicobacter pylori